Binding of neural cell adhesion molecules (N-CAMs) to the cellular prion protein

Hemin Interactions and Alterations of the Subcellular Localization of Prion Protein

“…2). Because hemin can interact with many proteins, we investigated the selectivity of the effects of hemin on the aggregation of PrP C compared with other cell surface proteins such as NCAM (neural cell adhesion molecule), which interacts with PrP C (31,32), and GFP-GPI protein, which follows default trafficking pathways of GPI anchored, lipid-raft-associated proteins (26). No hemin-induced alteration of NCAM or GFP-GPI solubility was observed, indicating a degree of specificity for the effects of hemin on PrP C solubility ( Fig.…”

“…2 and 4), which is also endocytosed by a clathrin-dependent mechanism in normal circumstances (58). Competition may occur between hemin and NCAM for the same binding site on PrP C because the N-terminal flexible domain of PrP C is involved in the binding of both hemin and NCAM (32). Furthermore, the induction of the formation of detergent-insoluble aggregates of PrP C by hemin (Fig.…”

“…Laminin (an extracellular matrix protein) (56), NCAM (a transmembrane adhesion molecule) (31,32), and STI-1 (a co-chaperone) (57) are important partners that assist in this function of PrP C . Interestingly, these ligands have distinct binding sites on the PrP C molecule and interact with PrP C on the cell surface suggesting that a formation of the macromolecular complex may occur on the plasma membrane in PrP C -dependent neuritogenesis.…”

New insights into cellular prion protein (PrPc) functions: The “ying and yang” of a relevant protein

“…However, only a small proportion of these related pathways are functional in a physiological context (see (Lee et al, 2003) or (Westergard et al, 2007) and (Linden et al, 2008) for reviews). Two in vitro studies demonstrate that PrP c binds to the laminin receptor 67K (Gauczynski et al, 2001) and the adhesion molecule N-CAM (Santuccione et al, 2005;Schmitt-Ulms et al, 2001), both transducing survival signals or promoting neurite outgrowth. In addition, PrP c mediates neuritogenesis in a laminin-mediated manner (Graner et al, 2000), thereby suggesting that the PrP c -laminin interaction is relevant for neuronal development and further plasticity-related mechanisms.…”

Absence of the Cellular Prion Protein Exacerbates and Prolongs Neuroinflammation in Experimental Autoimmune Encephalomyelitis

“…2,3 PrP C may serve as a receptor for a variety of putative ligands, including: heparan sulfate, 4 laminin, 5 neural cell adhesion molecule, 6 various synaptic proteins, 7 and stressinducible protein-1. 8 These ligand-receptor interactions suggest that PrP C could have a role in diverse processes, including neurodevelopment, synaptic function, neurite outgrowth, and neuronal survival.…”